1o7j

From Proteopedia

Revision as of 12:00, 30 October 2007

ATOMIC RESOLUTION STRUCTURE OF ERWINIA CHRYSANTHEMI L-ASPARAGINASE

Overview

An X-ray structure of L-asparaginase from Erwinia chrysanthemi (ErA) has, been refined at 1 A resolution to an R factor of below 0.1, using data, collected on a synchrotron source. With four molecules of the enzyme, consisting of 327 amino acids each, this crystal contains one of the, largest asymmetric units of a protein refined to date at atomic, resolution. Previously, structures of ErA and of related enzymes from, other bacterial sources have been refined at resolutions not exceeding 1.7, A; thus, the present structure represents a very significant improvement, in the quality of the available models of these proteins and should, provide a good basis for future studies of the conformational variability, of proteins, identification of subtle conformational features and, corroboration of ... [(full description)]

About this Structure

1O7J is a [Single protein] structure of sequence from [Erwinia chrysanthemi] with SO4, EDO and GOL as [ligands]. Active as [Asparaginase], with EC number [3.5.1.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Atomic resolution structure of Erwinia chrysanthemi L-asparaginase., Lubkowski J, Dauter M, Aghaiypour K, Wlodawer A, Dauter Z, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):84-92. Epub 2002, Dec 19. PMID:12499544

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